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Database: UniProt
Entry: Q30WJ6
LinkDB: Q30WJ6
Original site: Q30WJ6 
ID   FLGH_OLEA2              Reviewed;         234 AA.
AC   Q30WJ6;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   RecName: Full=Flagellar L-ring protein {ECO:0000255|HAMAP-Rule:MF_00415};
DE   AltName: Full=Basal body L-ring protein {ECO:0000255|HAMAP-Rule:MF_00415};
DE   Flags: Precursor;
GN   Name=flgH {ECO:0000255|HAMAP-Rule:MF_00415}; OrderedLocusNames=Dde_3156;
OS   Oleidesulfovibrio alaskensis (strain ATCC BAA-1058 / DSM 17464 / G20)
OS   (Desulfovibrio alaskensis).
OC   Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC   Desulfovibrionaceae; Oleidesulfovibrio.
OX   NCBI_TaxID=207559;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1058 / DSM 17464 / G20;
RX   PubMed=21685289; DOI=10.1128/jb.05400-11;
RA   Hauser L.J., Land M.L., Brown S.D., Larimer F., Keller K.L.,
RA   Rapp-Giles B.J., Price M.N., Lin M., Bruce D.C., Detter J.C., Tapia R.,
RA   Han C.S., Goodwin L.A., Cheng J.F., Pitluck S., Copeland A., Lucas S.,
RA   Nolan M., Lapidus A.L., Palumbo A.V., Wall J.D.;
RT   "Complete genome sequence and updated annotation of Desulfovibrio
RT   alaskensis G20.";
RL   J. Bacteriol. 193:4268-4269(2011).
CC   -!- FUNCTION: Assembles around the rod to form the L-ring and probably
CC       protects the motor/basal body from shearing forces during rotation.
CC       {ECO:0000255|HAMAP-Rule:MF_00415}.
CC   -!- SUBUNIT: The basal body constitutes a major portion of the flagellar
CC       organelle and consists of four rings (L,P,S, and M) mounted on a
CC       central rod. {ECO:0000255|HAMAP-Rule:MF_00415}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00415}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_00415}.
CC       Bacterial flagellum basal body {ECO:0000255|HAMAP-Rule:MF_00415}.
CC   -!- SIMILARITY: Belongs to the FlgH family. {ECO:0000255|HAMAP-
CC       Rule:MF_00415}.
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DR   EMBL; CP000112; ABB39950.1; -; Genomic_DNA.
DR   RefSeq; WP_011368904.1; NC_007519.1.
DR   AlphaFoldDB; Q30WJ6; -.
DR   SMR; Q30WJ6; -.
DR   STRING; 207559.Dde_3156; -.
DR   KEGG; dde:Dde_3156; -.
DR   eggNOG; COG2063; Bacteria.
DR   HOGENOM; CLU_069313_1_1_7; -.
DR   Proteomes; UP000002710; Chromosome.
DR   GO; GO:0009427; C:bacterial-type flagellum basal body, distal rod, L ring; IEA:InterPro.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003774; F:cytoskeletal motor activity; IEA:InterPro.
DR   GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IEA:InterPro.
DR   HAMAP; MF_00415; FlgH; 1.
DR   InterPro; IPR000527; Flag_Lring.
DR   PANTHER; PTHR34933; FLAGELLAR L-RING PROTEIN; 1.
DR   PANTHER; PTHR34933:SF1; FLAGELLAR L-RING PROTEIN; 1.
DR   Pfam; PF02107; FlgH; 1.
DR   PRINTS; PR01008; FLGLRINGFLGH.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Bacterial flagellum; Cell outer membrane; Lipoprotein; Membrane; Palmitate;
KW   Reference proteome; Signal.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00415"
FT   CHAIN           16..234
FT                   /note="Flagellar L-ring protein"
FT                   /id="PRO_0000236821"
FT   LIPID           16
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00415"
FT   LIPID           16
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00415"
SQ   SEQUENCE   234 AA;  25264 MW;  D1EA4BD06B50F7AE CRC64;
     MRYAVICMLL LAASGCTAAR QAPSPEPGLV PPPVVTTPEE KAENPGSLFS DENADLLYAD
     YRARRVGDIV LINIVENSKA ENKASTSTNK ESTGEYGVSS FFDRSKVGII PGQTLLSGRT
     GDVPLLKFSS VSDFSGDGET TRENTVTATI AARVTRVLPG GLMQVEGSRE TRVNEETQIV
     TVSGLVRTSD VADDNSVMST QMADARISYY GKGVISDKQR VGWFTRLMDN LWPF
//
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